Search results for "TLE"

showing 10 items of 2417 documents

Interaction of Doxorubicin with Polynucleotides. A Spectroscopic Study

2014

The interaction of doxorubicin (DX) with model polynucleotides poly(dG-dC)·poly(dG-dC) (polyGC), poly(dA-dT)·poly(dA-dT) (polyAT), and calf thymus DNA has been studied by several spectroscopic techniques in phosphate buffer aqueous solutions. UV-vis, circular dichroism, and fluorescence spectroscopic data confirm that intercalation is the prevailing mode of interaction, and also reveal that the interaction with AT-rich regions leads to the transfer of excitation energy to DX not previously documented in the literature. Moreover, the DX affinity for AT sites has been found to be on the same order of magnitude as that reported for GC sites.

Models MolecularCircular dichroismStereochemistryPolynucleotidesIntercalation (chemistry)polinucleotidi; spettroscopia; doxorubicinaBiochemistrychemistry.chemical_compoundSpectrophotometrymedicineAnimalsMoleculeAqueous solutionMolecular Structuremedicine.diagnostic_testChemistryCircular DichroismDNAFluorescenceCrystallographySpectrometry FluorescenceDoxorubicinPolynucleotideCattleSpectrophotometry UltravioletDNABiochemistry
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Pharmacogenomics of cantharidin in tumor cells.

2014

Cantharis vesicatoria (blister beetle) is used in Chinese medicine and has been categorized as highly toxic in the Chinese pharmacopeia. In Europe, Cantharis patches have been used since ages to treat various skin-related diseases. We investigated the cytotoxicity of the Cantharis ingredient, cantharidin, in 41 tumor cell lines (Oncotest panel) and compared the results with those of 60 cell lines of the National Cancer Institute, USA. We found profound activity at low micromolar concentrations (log ₁₀IC₅₀ values between -6.980 and 5.009 M). Cantharidin bound to protein phosphatase 2A (PP2A) with higher affinity (-8.12 kcal/mol) than to PP1 (-6.25 kcal/mol) in molecular docking analyses. Usi…

Models MolecularProtein ConformationBlister beetleBiologyCantharisBiochemistryFas ligandGene Expression Regulation Enzymologicchemistry.chemical_compoundCell Line TumorGene expressionAnimalsHumansRNA MessengerCytotoxicityOligonucleotide Array Sequence AnalysisPharmacologyCantharidinBinding SitesMolecular Structurebiology.organism_classificationMolecular biologyReceptors Neuropeptide YchemistryCell cultureApoptosisPharmacogeneticsImmunologyCantharidinBiochemical pharmacology
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Self-assembling of poly(aspartic acid) with bovine serum albumin in aqueous solutions

2016

Abstract Macromolecular co-assemblies built up in aqueous solutions, by using a linear polypeptide, poly(aspartic acid) (PAS), and a globular protein, bovine serum albumin (BSA), have been studied. The main interest was to identify the optimum conditions for an interpenetrated complex formation in order to design materials suitable for biomedical applications, such as drug delivery systems. BSA surface possesses several amino- and carboxylic groups available for covalent modification, and/or bioactive substances attachment. In the present study, mixtures between PAS and BSA were investigated at 37 °C in dilute aqueous solution by viscometry, dynamic light scattering and zeta potential deter…

Models MolecularProtein ConformationGlobular protein02 engineering and technology010402 general chemistry01 natural sciencesBiochemistryDynamic light scatteringStructural BiologyAspartic acidZeta potentialAnimalsBovine serum albuminMolecular Biologychemistry.chemical_classificationAqueous solutionChromatographybiologyChemistryWaterSerum Albumin BovineGeneral MedicineHydrogen-Ion Concentration021001 nanoscience & nanotechnology0104 chemical sciencesSolutionsDrug deliverybiology.proteinCattlePeptides0210 nano-technologyProtein BindingNuclear chemistryMacromoleculeInternational Journal of Biological Macromolecules
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Evidence for Water-Tuned Structural Differences in Proteins: An Approach Emphasizing Variations in Local Hydrophilicity

2012

We present experimental evidence for the significant effect that water can have on the functional structure of proteins in solution. Human (HSA) and Bovine Serum Albumin (BSA) have an amino acid sequence identity of 75.52% and are chosen as model proteins. We employ EPR-based nanoscale distance measurements using double electron-electron resonance (DEER) spectroscopy and both albumins loaded with long chain fatty acids (FAs) in solution to globally (yet indirectly) characterize the tertiary protein structures from the bound ligands' points of view. The complete primary structures and crystal structures of HSA and as of recently also BSA are available. We complement the picture as we have re…

Models MolecularProtein StructureMedical PhysicsNon-Clinical MedicineProtein ConformationMaterials ScienceBiophysicsMolecular Conformationlcsh:MedicineElectronsLigandsBiochemistryPhysical ChemistryAnalytical ChemistryMacromolecular Structure AnalysisAnimalsHumanslcsh:ScienceBiologySerum AlbuminQuantum MechanicsPhysicslcsh:RFatty AcidsElectron Spin Resonance SpectroscopyProteinsComputational BiologyWaterSerum Albumin BovineProtein Structure Tertiarybody regionsChemistrySpectrophotometryInterdisciplinary PhysicsMedicinelcsh:QMaterials CharacterizationCattleMedicinal ChemistryHydrophobic and Hydrophilic InteractionsResearch ArticleProtein BindingPLoS ONE
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Mechanisms of DNA damage by photoexcited 9-methyl-β-carbolines

2013

It has been well documented that β-carboline alkaloids, particularly the 9-methyl derivatives, are efficient photosensitizers. However, structure–activity relationships are missing and the photochemical mechanisms involved in the DNA photodamage still remain unknown. In the present work, we examined the capability of three 9-methyl-β-carbolines (9-methyl-norharmane, 9-methyl-harmane and 9-methylharmine) to induce DNA damage upon UVA excitation at physiological pH. The type and extent of the damage was analyzed together with the photophysical and binding properties of the β-carboline derivatives investigated. The results indicate that even at neutral pH most of the DNA damage is generated fr…

Models MolecularPurineUltraviolet RaysStereochemistryDNA damagePyrimidine dimerProtonationPhotochemistryBiochemistryCiencias Biológicaschemistry.chemical_compoundGenética y HerenciaAnimalsPhysical and Theoretical ChemistryPhotosensitizing AgentsChemistryCorticoviridaeOrganic ChemistryCiencias QuímicasDNASolventQuímica Orgánica9-methyl-b-carbolinesYield (chemistry)Excited stateDNA ViralCattlePhotosensitizationDNACIENCIAS NATURALES Y EXACTASCarbolinesDNA Damage
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Spectroscopic studies of the interaction of 3-(2-thienyl)-[1,2,3]triazolo[1,5-a]pyridine with 2,6-dimethyl-β-cyclodextrin and ctDNA

2016

The inclusion complexation behavior of 3-(2-thienyl)-[1,2,3]triazolo[1,5-a] pyridine (TTP) with native β-cyclodextrin and derivatized cyclodextrins was investigated. Stability constants for complexes with 1 : 1 molar ratios were calculated from phase solubility diagrams. The solubilizing efficiency of the TTP inclusion complex is enhanced in the order of DMβCD > HPβCD > βCD. The TTP-DMβCD inclusion complex was further characterized in solution by means of absorption, fluorescence, 2D NMR and molecular modeling methods. The thermodynamic studies indicate that the inclusion of TTP into the cyclodextrin cavity is mainly an enthalpy-driven process. The 2D NMR studies revealed that the thienyl m…

Models MolecularPyridinesStereochemistryIntercalation (chemistry)Antineoplastic Agents010402 general chemistry01 natural sciencesBiochemistryHydrophobic effectchemistry.chemical_compoundPyridineCarbohydrate ConformationAnimalsMoietyPhysical and Theoretical ChemistrySolubilitychemistry.chemical_classificationCyclodextrin010405 organic chemistrySpectrum Analysisbeta-CyclodextrinsOrganic ChemistryDNATriazoles0104 chemical sciencesCrystallographychemistryDocking (molecular)CattleTwo-dimensional nuclear magnetic resonance spectroscopyOrganic & Biomolecular Chemistry
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Structural requirements for V2 vasopressin receptor proteolytic cleavage.

1999

The ligand-induced proteolytic cleavage of the V2 vasopressin receptor transiently expressed in COS cells was investigated. After incubation of the cell membranes with a photoreactive ligand possessing full agonistic properties for V2 receptors, approximately 90% of the porcine and bovine V2 vasopressin receptors were cleaved in the upper part of transmembrane helix 2 at a heptapeptide sequence conserved in both vasopressin and oxytocin receptors. The oxytocin receptor was completely resistant to proteolysis after binding the same photoreactive ligand, which is only a partial agonist for this receptor. Chimeric V2/oxytocin receptors obtained by transfer of extracellular domains of the oxyto…

Models MolecularReceptors VasopressinDNA ComplementaryTime FactorsProtein ConformationSwineMolecular Sequence DataBiologyLigandsTransfectionBiochemistryArginine vasopressin receptor 2Enzyme-linked receptorCyclic AMPAnimalsHumansPoint Mutation5-HT5A receptorAmino Acid SequenceCloning MolecularReceptorProtease-activated receptor 2Vasopressin receptorArginine vasopressin receptor 1BDose-Response Relationship DrugSequence Homology Amino AcidProteinsOxytocin receptorProtein Structure TertiaryEnzyme ActivationBiochemistryMicroscopy FluorescenceReceptors OxytocinType C PhospholipasesCOS CellsMutagenesis Site-DirectedCattlehormones hormone substitutes and hormone antagonistsAdenylyl CyclasesProtein BindingEuropean journal of biochemistry
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Electrostatic control of the photoisomerization efficiency and optical properties in visual pigments: on the role of counterion quenching.

2009

Hybrid QM(CASPT2//CASSCF/6-31G*)/MM(Amber) computations have been used to map the photoisomerization path of the retinal chromophore in Rhodopsin and explore the reasons behind the photoactivity efficiency and spectral control in the visual pigments. It is shown that while the electrostatic environment plays a central role in properly tuning the optical properties of the chromophore, it is also critical in biasing the ultrafast photochemical event: it controls the slope of the photoisomerization channel as well as the accessibility of the S(1)/S(0) crossing space triggering the ultrafast decay. The roles of the E113 counterion, the E181 residue, and the other amino acids of the protein pock…

Models MolecularRhodopsinPhotoisomerizationPhotochemistryStatic ElectricityPhotochemistryCrystallography X-RayBiochemistryCatalysisRetinaProtein environmentColloid and Surface ChemistryIsomerismAnimalschemistry.chemical_classificationIonsBinding SitesbiologyColor VisionComputational BiologyBiasingGeneral ChemistryChromophoreVisual pigmentschemistryRhodopsinMutationbiology.proteinQuantum TheoryThermodynamicsCattleCounterionProtonsUltrashort pulseJournal of the American Chemical Society
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Atomic structure of the major capsid protein of rotavirus: implications for the architecture of the virion

2001

The structural protein VP6 of rotavirus, an important pathogen responsible for severe gastroenteritis in children, forms the middle layer in the triple-layered viral capsid. Here we present the crystal structure of VP6 determined to 2 A resolution and describe its interactions with other capsid proteins by fitting the atomic model into electron cryomicroscopic reconstructions of viral particles. VP6, which forms a tight trimer, has two distinct domains: a distal beta-barrel domain and a proximal alpha-helical domain, which interact with the outer and inner layer of the virion, respectively. The overall fold is similar to that of protein VP7 from bluetongue virus, with the subunits wrapping …

Models MolecularRotavirusCations DivalentViral proteinvirusesMolecular Sequence DataHemagglutinins ViralTrimerCrystal structureBiologyCrystallography X-Raymedicine.disease_causeProtein Structure SecondaryArticleGeneral Biochemistry Genetics and Molecular BiologyVirus03 medical and health sciencesCapsidRotavirusAtomic modelmedicineAnimalsAmino Acid SequenceAntigens ViralMolecular BiologyPeptide sequence030304 developmental biology0303 health sciencesSequence Homology Amino AcidGeneral Immunology and Microbiology030306 microbiologyViral Core ProteinsGeneral NeuroscienceVirionvirus diseasesMolecular biologyZincCapsidSolventsBiophysicsCapsid ProteinsCattleThe EMBO Journal
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3-acetylaltholactone and related styryl-lactones, mitochondrial respiratory chain inhibitors.

2000

A novel furano-pyrone, 3-acetylaltholactone, and two other known styryl-lactones, altholactone and 5-acetoxyisogoniothalamin oxide, have been isolated from Goniothalamus arvensis (Annonaceae) stem bark. We report here the isolation and structural elucidation of these compounds with furane-pyrone and styryl-pyrone skeletons, postulating also for the first time their mechanism of cytotoxicity based on inhibition on mammalian mitochondrial respiratory chain.

Models MolecularStereochemistryChemical structureSubmitochondrial ParticlesMolecular ConformationPlant ScienceHorticultureBiochemistryMitochondria HeartStyrenesLactonesOxygen ConsumptionAnimals3-acetylaltholactoneCytotoxicityFuransMolecular BiologyGoniothalamusStem barkPlants MedicinalbiologyMolecular StructurePlant StemsUncoupling AgentsGeneral Medicinebiology.organism_classificationNADKineticsMitochondrial respiratory chainAnnonaceaePyronesvisual_artvisual_art.visual_art_mediumBarkCattlePhytochemistry
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